Editor 3.0: Redesigining the YAWL user interface

It has long been a concern that the wider uptake of the YAWL environment may have been hindered by the usability issues identified in the current Process Editor. As a consequence, it was decided that the Editor be completely rewritten to address those usability limitations. The result has been the implementation of a new YAWL Process Editor architecture that creates a clear separation between the User Interface component layer and the core processing back end, facilitating the redesign of the default user interface. This new architecture also supports the development of multiple User Interface front ends for specific contexts that take advantage of the core capabilities the new Editor architecture has to offer.

Evidence for the adsorption of molecules at special sites located at copper/zinc oxide interfaces. Part 3. -- Fourier-transform infrared study of methyl formate adsorption on reduced and oxidised Cu/ZnO/SiO2 catalysts

FTIR spectra are reported of methyl formate adsorbed at 295 K on ZnO/SiO2, reduced Cu/ZnO/SiO2 and on Cu/ZnO/SiO2 which had been preoxidised by exposure to nitrous oxide. Methyl formate on ZnO/SiO2 gave adsorbed zinc formate species and strongly physisorbed molecular methanol on silica. The comparable reaction of methyl formate with reduced Cu/ZnO/SiO2 catalyst produced bridging formate species on copper and a diminished quantity of zinc formate relative to that formed on ZnO/SiO2 catalyst. This effect is explained in terms of site blockage on the ZnO surface by small copper clusters. Addition of methyl formate to a reoxidised Cu/ZnO/SiO2 catalyst produced a considerably greater amount of formate species on zinc oxide and methoxy groups on copper were detected. The increase in concentration of zinc formate species was rationalised in terms of rearrangement of unidentate copper formate species to become bonded to copper and zinc oxide sites located at the interface between these two components.

Molecular cocrystals of 5-(4-bromophenyl)-1,3,4-thiadiazol-2-amine: hydrogen bonding in the structures of the 1:1 adduct with 2-(naphthalen-2-yloxy)acetic acid and the salt with 3,5-dinitrobenzoic acid

The structures of the anhydrous products from the interaction of 2-amino-5-(4-bromophenyl)-1,3,4-thiadiazole with (2-naphthoxy)acetic acid, the 1:1 adduct C8H6BrN3S . C12H10O3 (I) and 3,5-dinitrobenzoic acid, the salt C8H7BrN3S+ C7H3N2O6- (II) have been determined. In the adduct (I), a heterodimer is formed through a cyclic hydrogen-bonding motif [graph set R2/2(8)], involving carboxylic acid O-H...N(hetero)and amine N-H...O(carboxyl) interactions. The heterodimers are essentially planar with a thiadiazole to naphthyl ring dihedral angle of 15.9(2)deg. and the intramolecular thiadiazole to phenyl ring angle of 4.7(2)deg. An amine N-H...N(hetero) hydrogen bond between the heterodimers generates a one-dimensional chain structure extending down [001]. Also present are weak benzene-benzene and naphthalene-naphthalene pi-pi stacking interactions down the b axis [minimum ring centroid separation, 3.936(3) Ang.]. With the salt (II), the cation-anion association is also through a cyclic R2/2(8) motif but involving duplex N-H...O(carboxyl) hydrogen bonds, giving a heterodimer which is close to planar [dihedral angles between the thiadiazole ring and the two benzene rings, 5.00(16)deg. (intra) and 7.23(15)deg. (inter)]. A secondary centrosymmetric cyclic N-H...O(carboxyl) hydrogen-bonding association involving the second amino H-atom generates a heterotetramer. Also present in the crystal are weak pi-pi i-\p interactions between thiadiazolium rings [minimum ring centroid separation, 3.936(3)Ang.], as well as a short Br...O(nitro) interaction [3.314(4)Ang.]. The two structures reported here now provide a total of three crystallographically characterized examples of co-crystalline products from the interaction of 2-amino-5-(4-bromophenyl)-1,3,4-thiadiazole with carboxylic acids, of which only one involves proton-transfer.

Analysis of 3 common polymorphisms in the KCNK18 gene in an Australian migraine case-control cohort

Migraine is a common neurological disorder characterised by temporary disabling attacks of severe head pain and associated disturbances. There is significant evidence to suggest a genetic aetiology to the disease however few causal mutations have been conclusively linked to the migraine subtypes Migraine with (MA) or without Aura (MO). The Potassium Channel, Subfamily K, member 18 (KCNK18) gene, coding the potassium channel TRESK, is the first gene in which a rare mutation resulting in a non-functional truncated protein has been identified and causally linked to MA in a multigenerational family. In this study, three common polymorphisms in the KCNK18 gene were analysed for genetic variation in an Australian case-control migraine population consisting of 340 migraine cases and 345 controls. No association was observed for the polymorphisms examined with the migraine phenotype or with any haplotypes across the gene. Therefore even though the KCNK18 gene is the only gene to be causally linked to MA our studies indicate that common genetic variation in the gene is not a contributor to MA.